HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Köhl, W. Articles by Herrler, G. Search for Related Content PubMed PubMed Citation Articles by Köhl, W. Articles by Herrler, G. Agricola Articles by Köhl, W. Articles by Herrler, G.

The surface glycoprotein E2 of bovine viral diarrhoea virus contains an intracellular localization signal

Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany

Correspondence
Georg Herrler
Georg.Herrler{at}tiho-hannover.de

The intracellular transport of the surface glycoprotein E2 of bovine viral diarrhoea virus was analysed by expressing the cloned gene in the absence of other viral proteins. Immunofluorescence analysis and surface biotinylation indicated that E2 is located in an early compartment of the secretory pathway and not transported to the cell surface. In agreement with this result, E2 was found to contain only high-mannose oligosaccharide side-chains but no N-glycans of the complex type. To define the intracellular localization signal of the E2 protein, chimeric proteins were generated. E2 chimeras containing the MT (membrane anchor plus carboxy-terminal domain) of the G protein of vesicular stomatitis virus (VSV) or of the F protein of bovine respiratory syncytial virus (BRSV) were transported to the cell surface. On the other hand, VSV G protein containing the MT domain of E2 was detected only in the ER, indicating that this domain contains an ER localization signal. A chimeric E2 protein, in which not the membrane anchor but only the carboxy-terminal end was replaced by the corresponding domain of the BRSV F protein, was also localized in the ER. Therefore, it was concluded that the membrane anchor contains the ER localization signal of E2. Interestingly, the ER export signal within the VSV G protein cytoplasmic tail was found to overrule the ER localization signal in the E2 protein membrane anchor.

This article has been cited by other articles:

				S. Ronecker, G. Zimmer, G. Herrler, I. Greiser-Wilke, and B. Grummer Formation of bovine viral diarrhea virus E1-E2 heterodimers is essential for virus entry and depends on charged residues in the transmembrane domains J. Gen. Virol., September 1, 2008; 89(9): 2114 - 2121. [Abstract] [Full Text] [PDF]

				W. Kohl, A. Grone, V. Moennig, and G. Herrler Expression of the surface glycoprotein E2 of Bovine viral diarrhea virus by recombinant vesicular stomatitis virus J. Gen. Virol., January 1, 2007; 88(1): 157 - 165. [Abstract] [Full Text] [PDF]

				A. Hanika, B. Larisch, E. Steinmann, C. Schwegmann-Wessels, G. Herrler, and G. Zimmer Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes J. Gen. Virol., May 1, 2005; 86(5): 1455 - 1465. [Abstract] [Full Text] [PDF]

				C. Schwegmann-Wessels, M. Al-Falah, D. Escors, Z. Wang, G. Zimmer, H. Deng, L. Enjuanes, H. Y. Naim, and G. Herrler A Novel Sorting Signal for Intracellular Localization Is Present in the S Protein of a Porcine Coronavirus but Absent from Severe Acute Respiratory Syndrome-associated Coronavirus J. Biol. Chem., October 15, 2004; 279(42): 43661 - 43666. [Abstract] [Full Text] [PDF]